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Database: UniProt/SWISS-PROT
Entry: F16PC_STRA1
LinkDB: F16PC_STRA1
Original site: F16PC_STRA1 
ID   F16PC_STRA1             Reviewed;         643 AA.
AC   Q3K2F6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
DE            Short=FBPase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
DE            EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01854};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 3 {ECO:0000255|HAMAP-Rule:MF_01854};
GN   Name=fbp {ECO:0000255|HAMAP-Rule:MF_01854}; OrderedLocusNames=SAK_0666;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01854};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01854};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01854}.
CC   -!- SIMILARITY: Belongs to the FBPase class 3 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01854}.
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DR   EMBL; CP000114; ABA46271.1; -; Genomic_DNA.
DR   RefSeq; WP_000064640.1; NC_007432.1.
DR   AlphaFoldDB; Q3K2F6; -.
DR   KEGG; sak:SAK_0666; -.
DR   HOGENOM; CLU_028392_2_0_9; -.
DR   UniPathway; UPA00138; -.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_01854; FBPase_class3; 1.
DR   InterPro; IPR009164; FBPtase_class3.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF06874; FBPase_2; 1.
DR   PIRSF; PIRSF000906; FBPtase_Bacill; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Manganese.
FT   CHAIN           1..643
FT                   /note="Fructose-1,6-bisphosphatase class 3"
FT                   /id="PRO_0000363112"
SQ   SEQUENCE   643 AA;  74921 MW;  F687C2C2453BE4DA CRC64;
     MSNFYKLLKE KFPRKEDIVT EMINLEAICQ LPKGTEYFIS DLHGEYDAVD YLLRTGAGSI
     RAKLLDCFDW QKIVAVDLDD FCILLYYPKE KLAFDKMNLS ASAYKTKLWE MIPLQIQVLK
     YFSSKYTKSK VRKQLSGKFA YIIEELLAEI DRNPEKKSYF DTIIEKLFEL DQVEDLIIVL
     SQTIQVLIID HLHVVGDIYD RGRYPDRILN RLMAFPNLDI QWGNHDVTWM GAASGSYLCM
     VNVIRIAARY NNITLIEDRY GINLRRLVDY SRRYYEPLPS FVPILDGEEM THPDELDLLN
     MIQQATAILQ FKLEAQLIDR RPEFQMHNRQ LINQVNYKDL SISIKEVVHQ LKDFNSRCID
     SKNPSRLTSE EEELLQQLMI AFQTSESLKK HIDFLFEKGS MYLTYNDNLL FHGCIPMHSN
     GDFKSFKIAG KTYGGRDLLD LFESQIRLAY ARPEKHDDLA TDIIWYLWCG ENSSLFGKNA
     MTTFERYYVS DKVTHQERKN PYFKLRDKDD ICTALLQEFD LPKFGHIVNG HTPVKEKNGE
     QPIKANGKML VIDGGFAKGY QKNTGLAGYT LIYNSYGIQL ISHLPFTSIE EVLSGTNYII
     DTKRLVEEAK DRILVKDTTI GQKLTKEIKD LDHLYRHFQE YDD
//
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